6lp0

crystal structure of alpha-momorcharin in complex with AMP

Method: X-RAY DIFFRACTION Dmax: 63.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ribosome-inactivating protein momordin I

OrganismNot specified

UniProt P16094

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–286 Not recorded AMP ADENOSINE MONOPHOSPHATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.2 M Magnesium Acetate, 20% PEG 8000, 0.1 M Sodium cacodylate, pH 6.5 Resolution 1.52 Å R-free 0.299

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RIP1_MOMCH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–286; UniProt 1–286

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6lp0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6lp0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6lp0
Deposition date deposition_date2020-01-07
Structure title titlecrystal structure of alpha-momorcharin in complex with AMP
Keywords keywordsalpha-momorcharin, ribosome-inactivating protein, rRNA N-glycosidase, AMP, PLANT PROTEIN; PLANT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.00
Radius of gyration Rg (electron density) rg_electron17.76
Forward intensity I(0) i013342100.00
Molecular weight molecular_weight27795.0 kDa
Excluded volume excluded_volume35026 ų
Envelope volume envelope_volume39709 ų
Hydration-shell volume shell_volume18518 ų
Envelope diameter envelope_diameter65.8
Shell Rg shell_rg24.21
Envelope Rg envelope_rg18.18
Shape Rg shape_rg17.74
Total Rg total_rg18.80
Total atoms total_atoms1961
Residues n_residues245
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax63.0
Rg (real space) rg_real18.92
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.3340e+07
I(0) uncertainty (real space) i0_real_error1.6040e+05
Rg (reciprocal space) rg_reciprocal18.93
I(0) (reciprocal space) i0_reciprocal13340000.0000
Solution quality estimate total_estimate0.7952
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.227
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3478000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.781; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6lp0a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.165 — Ribosome inactivating proteins (RIP)
Superfamily Superfamily superfamilyd.165.1 — Ribosome inactivating proteins (RIP)
Family Family familyd.165.1.0 — automated matches

8. Citations (1)

9. Files and Curves (10)